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Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization
TLDR
The molecular basis of chitin recognition by the rice receptor, CEBiP (chitin-elicitor binding protein), and following receptor dimerization is shown based on the results of biochemical studies, epitope mapping by saturation transfer difference NMR spectroscopy and molecular modeling/docking studies. Expand
Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. tuberculosis.
TLDR
Interestingly, sequence comparisons indicate that these structural features are also shared by G5 domains involved in biofilm formation, which suggests that the RpfB G5 domain has a cell-wall adhesive function, which allows the catalytic domain to be properly oriented for the cleavage reaction. Expand
A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping
TLDR
This review provides an update of the structural and functional data on the key actors of the replicatory machinery of SARS-CoV-2, to fill the gaps in the currently available structural data, which is mainly obtained through homology modeling. Expand
Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses.
TLDR
The crystal structure of RpfB catalytic domain in complex with N,N',N"-triacetyl-chitotriose provides the first, to the authors' knowledge, atomic representation of ligand recognition by R pfB and demonstrates that the strongest interactions are established by the N-acetylglucosamine moiety in the central region of the enzyme binding cleft. Expand
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
TLDR
X-ray structural results obtained in the present study provide molecular clues into the mechanism of muropeptide-induced PrkC activation and show that EC-PrkC shows no tendency to dimerize even in the presence of high concentrations of m Kuropeptides. Expand
A 35 kDa NAD(P)H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase.
TLDR
The findings indicate that SsTrxR is structurally related to the class II of the pyridine nucleotide-disulphide oxidoreductases family and exhibits a NADP(H) dependent thioredoxin reductase activity requiring the presence of FAD. Expand
Characterisation of the components of the thioredoxin system in the archaeon Sulfolobus solfataricus
TLDR
Characterisation of a Trx-B from the hyperthermophile Sulfolobus solfataricus and the determination of the redox potential of the thioredoxin system in S. solfatonicus will contribute to add further information on this key enzyme system in Archaea. Expand
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy.
TLDR
This work exploited the structural requirements necessary for recognition and binding and proved that muropeptides physically bind to EC-PrkC through DAP-moiety-mediated interactions with an arginine residue, Arg500, belonging to the protein C-terminal PASTA domain. Expand
Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation.
TLDR
The crystal structure of a relevant portion of RipA, containing its catalytic-domain and an extra-domain of hitherto unknown function, is reported, providing the first evidence of self-inhibition in cell-disconnecting enzymes and opens a field for the design of novel antitubercular therapeutics. Expand
A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria
TLDR
The current study provides the first insights into the molecular mechanism of resuscitation from dormancy involving a product of RpfB/RipA‐mediated peptidoglycan cleavage. Expand
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